ArticleJournal of virology1997
Active-site residues of cyclophilin A are crucial for its incorporation into human immunodeficiency virus type 1 virions.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 46 citations in OpenAlex.
- Precision Editing of Cyclophilin A Generates Cyclosporine and Voclosporin Resistant Cellular Therapies.Blood immunology & cellular therapy · 2026Article
- Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.PLoS pathogens · 2024Article
- GC-MS Analysis, Antibacterial, and Anticancer Activities ofMicroorganisms · 2023Article
- Repurposing of cyclophilin A inhibitors as broad-spectrum antiviral agents.Drug discovery today · 2022Review
- The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink.Journal of the American Chemical Society · 2022Article
- Comparative genetic variability in HIV-1 subtype C p24 Gene in early age groups of infants.Virus genes · 2018Article
- Function of Cyclophilin1 as a long-distance signal molecule in the phloem of tomato plants.Journal of experimental botany · 2017Article
- The role of immunophilins in viral infection.Biochimica et biophysica acta · 2015Article
- Genetic deficiency and polymorphisms of cyclophilin A reveal its essential role for Human Coronavirus 229E replication.Current opinion in virology · 2015Review
- Cyclophilin A promotes HIV-1 reverse transcription but its effect on transduction correlates best with its effect on nuclear entry of viral cDNA.Retrovirology · 2014Article
- Antiviral activity of recombinant ankyrin targeted to the capsid domain of HIV-1 Gag polyprotein.Retrovirology · 2012Article
- Productive replication and evolution of HIV-1 in ferret cells.Journal of virology · 2012Article
- The host-pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains.BMC structural biology · 2011Article
- The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.BMC structural biology · 2010Article
- Rescue of HIV-1 release by targeting widely divergent NEDD4-type ubiquitin ligases and isolated catalytic HECT domains to Gag.PLoS pathogens · 2010Article
- Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.PLoS biology · 2010Article
- Article
- Analysis of human cell heterokaryons demonstrates that target cell restriction of cyclosporine-resistant human immunodeficiency virus type 1 mutants is genetically dominant.Journal of virology · 2007Article
- Structure-based identification of small molecule compounds targeting cell cyclophilin A with anti-HIV-1 activity.European journal of pharmacology · 2007Article
- One novel quinoxaline derivative as a potent human cyclophilin A inhibitor shows highly inhibitory activity against mouse spleen cell proliferation.Bioorganic & medicinal chemistry · 2006Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human immunodeficiency virus type 1 (HIV-1) incorporates the cellular peptidyl-prolyl cis-trans isomerase cyclophilin A (CyPA), the cytosolic receptor for the immunosuppressant cyclosporin A (CsA). CsA inhibits the incorporation of CyPA and reduces HIV-1 virion infectivity but is inactive against closely related primate lentiviruses that do not interact with CyPA. The incorporation of CyPA into HIV-1 virions is mediated by a specific interaction with a proline-containing, solvent-exposed loop in the capsid (CA) domain of the Gag polyprotein. CsA, which disrupts the interaction with CA, binds at the active site of CyPA. To test whether active-site residues are also involved in the interaction with HIV-1 CA, we used a panel of previously characterized active-site mutants of human CyPA. Expression vectors for epitope-tagged wild-type and mutant CyPA were transfected into COS-gamma cells along with HIV-1 proviral DNA, and the virions produced were analyzed for the presence of tagged proteins. Cotransfection of the wild-type expression vector led to the incorporation of readily detectable amounts of epitope-tagged CyPA into HIV-1 virions. One CyPA mutant with a substantially decreased sensitivity to CsA was incorporated with wild-type efficiency, demonstrating that the requirements for binding to CsA and to HIV-1 CA are not identical. The remaining six CyPA mutants were incorporated with markedly reduced efficiency, providing in vivo evidence that HIV-1 CA interacts with the active site of CyPA.
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